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Volumn 119, Issue 41, 1997, Pages 9729-9737

Electrochemical potential and pH dependences of [3Fe-4S] ⇆ [M3Fe-4S] cluster transformations (M = Fe, Zn, Co, and Cd) in ferredoxin III from Desulfovibrio africanus and detection of a cluster with M = Pb

Author keywords

[No Author keywords available]

Indexed keywords

CADMIUM; COBALT; FERREDOXIN; IRON; METAL COMPLEX; ZINC;

EID: 0030665158     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja971403a     Document Type: Article
Times cited : (38)

References (73)
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    • For other examples of the applications of protein film voltammetry in enzymology and bioinorganic chemistry, and specifically for the study of redox-coupled reactions, see: (a) Sucheta, A; Ackrell, B. A. C.; Cochran, B.; Armstrong, F. A. Nature 1992, 356, 361-362. (b) Sucheta; A.; Cammack, R.; Weiner, J.; Armstrong, F. A. Biochemistry 1993, 32, 5455-5465. (c) Butt, J. N.; Sucheta, A.; Martin, L. L.; Shen, B.; Burgess, B. K.; Armstrong, F. A. J. Am. Chem. Soc. 1993, 115, 12587-12588, (d) Mondal, M. S.; Fuller, H. A.; Armstrong, F. A. J. Am. Chem. Soc. 1996, 118, 263-264. (e) Hirst, J.; Sucheta, A.; Ackrell, B. A. C.; Armstrong, F. A. J. Am. Chem. Soc. 1996, 118, 5031-5038. (f) Hirst, J.; Ackrell, B. A. C.; Armstrong, F. A. J. Am. Chem. Soc. 1997, 119, 7434-7439. (g) Armstrong, F. A. In Bioelectrochemistry of Biomacromolecules (Volume 5 of Bioelectrochemistry: Principles and Practice); Lenaz, G., Milazzo, G., Eds.; Birkhauser: 1992; pp 205-255. (h) Heering, H. A.; Hirst, J.; Armstrong, F. A. Chem. Soc. Rev. 1997, 26, 169-179.
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    • For other examples of the applications of protein film voltammetry in enzymology and bioinorganic chemistry, and specifically for the study of redox-coupled reactions, see: (a) Sucheta, A; Ackrell, B. A. C.; Cochran, B.; Armstrong, F. A. Nature 1992, 356, 361-362. (b) Sucheta; A.; Cammack, R.; Weiner, J.; Armstrong, F. A. Biochemistry 1993, 32, 5455-5465. (c) Butt, J. N.; Sucheta, A.; Martin, L. L.; Shen, B.; Burgess, B. K.; Armstrong, F. A. J. Am. Chem. Soc. 1993, 115, 12587-12588, (d) Mondal, M. S.; Fuller, H. A.; Armstrong, F. A. J. Am. Chem. Soc. 1996, 118, 263-264. (e) Hirst, J.; Sucheta, A.; Ackrell, B. A. C.; Armstrong, F. A. J. Am. Chem. Soc. 1996, 118, 5031-5038. (f) Hirst, J.; Ackrell, B. A. C.; Armstrong, F. A. J. Am. Chem. Soc. 1997, 119, 7434-7439. (g) Armstrong, F. A. In Bioelectrochemistry of Biomacromolecules (Volume 5 of Bioelectrochemistry: Principles and Practice); Lenaz, G., Milazzo, G., Eds.; Birkhauser: 1992; pp 205-255. (h) Heering, H. A.; Hirst, J.; Armstrong, F. A. Chem. Soc. Rev. 1997, 26, 169-179.
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    • note
    • 2+/1+ couple in the film and in solution is somewhat greater than typically observed for this protein (<20 mV).
  • 57
    • 1842299164 scopus 로고    scopus 로고
    • note
    • 4}
  • 58
    • 1842409432 scopus 로고    scopus 로고
    • note
    • 1+, and signals at g = 5.3, 2.4 due to Co(II)EGTA.
  • 65
    • 1842365913 scopus 로고    scopus 로고
    • note
    • 2- state formed in other proteins, e.g., Sulfolobus acidocatdarius Fd is more stable.
  • 66
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    • The presence of EGTA in M-release experiments is probably more important for metal ions that bind very tightly to the cluster, thereby necessitating sequestration of even trace contaminating levels.
    • The presence of EGTA in M-release experiments is probably more important for metal ions that bind very tightly to the cluster, thereby necessitating sequestration of even trace contaminating levels.
  • 67
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    • note
    • 2-.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.